Catalase - Proteus mirabilis

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Reviewed, UniProtKB/Swiss-Prot P42321 (CATA_PROMI)

Last modified June 16, 2009. Version 70. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:

katA

Organism

Proteus mirabilis

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H₂O₂ = O₂ + 2 H₂O.
Cofactor	Heme group. NADP.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the catalase family.
Mass spectrometry	Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. Ref.1

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Oxidation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

484

Catalase

PRO_0000084992

Sites

Active site

1

Active site

1

Metal binding

1

Iron (heme axial ligand) Ref.2

Amino acid modifications

Modified residue

1

Methionine sulfone

Secondary structure

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484

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P42321-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: ADC25F3CB41F5C50
Show »

484

55,614

        10         20         30         40         50         60 
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA 

        70         80         90        100        110        120 
FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG AADAERDIRG FALKFYTEEG 

       130        140        150        160        170        180 
NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS 

       190        200        210        220        230        240 
DRGLPLSYRF VHGFGSHTYS FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS 

       250        260        270        280        290        300 
QRDLFEAIER GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN 

       310        320        330        340        350        360 
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH QIPVNAPKCP 

       370        380        390        400        410        420 
FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP LSIEGAADHW NHREDEDYFS 

       430        440        450        460        470        480 
QPRALYELLS DDEHQRMFAR IAGELSQASK ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG 


KDAK

References

[1]	"Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site." Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G. J. Protein Chem. 14:59-72(1995) [PubMed: 7786407] [Abstract] Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, MASS SPECTROMETRY. Strain: PR.
[2]	"Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH." Gouet P., Jouve H.-M., Dideberg O. J. Mol. Biol. 249:933-954(1995) [PubMed: 7791219] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). Strain: PR.
[3]	"Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy." Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J. Nat. Struct. Biol. 3:951-956(1996) [PubMed: 8901874] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ABSORPTION SPECTROSCOPY.
[4]	"High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron." Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M. Proteins 50:261-271(2003) [PubMed: 12486720] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), EPR SPECTROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E93	X-ray	2.00	A	1-484	[»]
1H6N	X-ray	2.11	A	1-484	[»]
1H7K	X-ray	2.40	A	2-484	[»]
1M85	X-ray	2.00	A	1-484	[»]
1MQF	X-ray	2.50	A	1-484	[»]
1NM0	X-ray	2.30	A	1-484	[»]
2CAG	X-ray	2.70	A	1-484	[»]
2CAH	X-ray	2.70	A	1-484	[»]

ModBase

Enzyme and pathway databases

BRENDA

Family and domain databases

InterPro

IPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]

Gene3D

G3DSA:2.40.180.10. Catalase_N. 1 hit.

PANTHER

PTHR11465. Catalase. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]

PRINTS

PR00067. CATALASE.

ProDom

PD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

CATA_PROMI

Accession

Primary (citable) accession number: P42321

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents